Výsledky vyhledávání

Identification of incompletely processed potential carboxypeptidase E substrates from CpEfat/CpEfat mice

Autor: E J, Bures, P L, Courchesne, J, Douglass, K, Chen, M T, Davis, M D, Jones, M D, McGinley, J H, Robinson, C S, Spahr, J, Sun, R C, Wahl, S D, Patterson

Publikováno v: Proteomics. 1(1)

In an attempt to identify peptides that may be involved in the obese phenotype observed in CpEfat/CpEfat mice (deficient in Carboxypeptidase E, CpE) samples from fourteen neuroendocrine tissues in wild-type and CpEfat/CpEfat mice were obtained. Pepti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::40b9aaef05be28d875d06537227ed467
https://pubmed.ncbi.nlm.nih.gov/11680901

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Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. II. Limitations of complex mixture analyses

Autor: M T, Davis, C S, Spahr, M D, McGinley, J H, Robinson, E J, Bures, J, Beierle, J, Mort, W, Yu, R, Luethy, S D, Patterson

Publikováno v: Proteomics. 1(1)

With an emphasis on obtaining a multitude of high quality tandem mass spectrometry spectra for protein identification, instrumental parameters are described for the liquid chromatography-tandem mass spectrometry analysis of trypsin digested unfractio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a1d74a36efefda14792c7df83fff800d
https://pubmed.ncbi.nlm.nih.gov/11680890

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Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest

Autor: C S, Spahr, M T, Davis, M D, McGinley, J H, Robinson, E J, Bures, J, Beierle, J, Mort, P L, Courchesne, K, Chen, R C, Wahl, W, Yu, R, Luethy, S D, Patterson

Publikováno v: Proteomics. 1(1)

The proteome of normal male urine from a commercial pooled source has been examined using direct liquid chromatography-tandem mass spectrometry (LC-MS/MS). The entire urinary protein mixture was denatured, reduced and enzymatically digested prior to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e6496b51f5f86b685adb5fd2378ce7a1
https://pubmed.ncbi.nlm.nih.gov/11680902

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Simplification of complex peptide mixtures for proteomic analysis: reversible biotinylation of cysteinyl peptides

Autor: C S, Spahr, S A, Susin, E J, Bures, J H, Robinson, M T, Davis, M D, McGinley, G, Kroemer, S D, Patterson

Publikováno v: Electrophoresis. 21(9)

A rapid means of identifying many components in an enriched mixture of proteins is enzymatic digestion of the entire protein fraction. This complex peptide mixture is then subjected to reversed-phase high performance liquid chromatography (HPLC) coup

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::494bf9c1426c5c81b90b4480f4b45c66
https://pubmed.ncbi.nlm.nih.gov/10870950

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A simplified device for protein identification by microcapillary gradient liquid chromatography-tandem mass spectrometry

Autor: M D, McGinley, M T, Davis, J H, Robinson, C S, Spahr, E J, Bures, J, Beierle, J, Mort, S D, Patterson

Publikováno v: Electrophoresis. 21(9)

A simplified device and procedure have been developed for microcapillary gradient liquid chromatography-tandem mass spectrometry (LC-MS/MS). This procedure has proved useful in identifying low level quantities of proteins from sodium dodecyl sulfate-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8a86153f9f55850a4527340f00aff9a9
https://pubmed.ncbi.nlm.nih.gov/10870954

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Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain

Autor: M, Haniu, T, Arakawa, E J, Bures, Y, Young, J O, Hui, M F, Rohde, A A, Welcher, T, Horan

Publikováno v: The Journal of biological chemistry. 273(44)

The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases. The extracellular domain of this receptor is comprised of two immuno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9304d3d44a6fbe494adae01b1465b275
https://pubmed.ncbi.nlm.nih.gov/9786864

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Interactions between brain-derived neurotrophic factor and the TRKB receptor. Identification of two ligand binding domains in soluble TRKB by affinity separation and chemical cross-linking

Autor: M, Haniu, S, Montestruque, E J, Bures, J, Talvenheimo, R, Toso, S, Lewis-Sandy, A A, Welcher, M F, Rohde

Publikováno v: The Journal of biological chemistry. 272(40)

The extracellular domain of the human neurotrophin TRKB receptor expressed in Chinese hamster ovary cells is a highly glycosylated protein, possessing binding ability for brain-derived neurotrophic factor (BDNF). Two distinct ligand binding domains o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8151695a077ec884d4a35270a9766a40
https://pubmed.ncbi.nlm.nih.gov/9312147

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Design, synthesis, and characterization of a protein sequencing reagent yielding amino acid derivatives with enhanced detectability by mass spectrometry

Autor: R, Aebersold, E J, Bures, M, Namchuk, M H, Goghari, B, Shushan, T C, Covey

Publikováno v: Protein science : a publication of the Protein Society. 1(4)

We report the design, chemical synthesis, and structural and functional characterization of a novel reagent for protein sequence analysis by the Edman degradation, yielding amino acid derivatives rapidly detectable at high sensitivity by ion-evaporat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6f0b6016fb7a590d1ddf20db1aed9960
https://pubmed.ncbi.nlm.nih.gov/1304351

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